Signals that Regulate GLUT4 Translocation

Signals that Regulate GLUT4 Translocation J. Membrane Biol. 190, 167–174 (2002) DOI: 10.1007/s00232-002-1035-3 Topical Review J.S. Elmendorf Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Center for Diabetes Research, 635Barnhill Dr., Indianapolis, IN 46202, USA Received: 24 May 2002/Accepted: 10 July 2002 Introduction Signal Transduction from the Insulin Receptor Removal of excess glucose from the circulation in- Insulin binding to the insulin receptor causes tyrosine volves the stimulation of glucose transport into autophosphorylation of the b-subunit and activation muscle and adipose tissue. In these tissues, the in- of its intrinsic tyrosine kinase (Fig. 1) (Cheatham & crease in glucose uptake depends on the redistribu- Kahn, 1995). The insulin receptor tyrosine kinase tion of intracellular vesicles containing the insulin- phosphorylates several intracellular proteins, includ- responsive glucose transporter GLUT4 to the cell ing the insulin receptor substrate (IRS) proteins that surface membrane by a process called translocation. provide docking sites for p85, the regulatory subunit These plasma membrane-localized transporters sub- of type I phosphatidylinositol 3-kinase (PI3K). This sequently facilitate the influx of plasma glucose into results in the activation of the catalytic p110 subunit the cell. Recent insights into this regulated process of PI3K. Multiple studies using various pharmaco- show that, in addition http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Signals that Regulate GLUT4 Translocation

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Publisher
Springer-Verlag
Copyright
Copyright © 2002 by Springer-Verlag New York Inc.
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-002-1035-3
Publisher site
See Article on Publisher Site

Abstract

J. Membrane Biol. 190, 167–174 (2002) DOI: 10.1007/s00232-002-1035-3 Topical Review J.S. Elmendorf Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Center for Diabetes Research, 635Barnhill Dr., Indianapolis, IN 46202, USA Received: 24 May 2002/Accepted: 10 July 2002 Introduction Signal Transduction from the Insulin Receptor Removal of excess glucose from the circulation in- Insulin binding to the insulin receptor causes tyrosine volves the stimulation of glucose transport into autophosphorylation of the b-subunit and activation muscle and adipose tissue. In these tissues, the in- of its intrinsic tyrosine kinase (Fig. 1) (Cheatham & crease in glucose uptake depends on the redistribu- Kahn, 1995). The insulin receptor tyrosine kinase tion of intracellular vesicles containing the insulin- phosphorylates several intracellular proteins, includ- responsive glucose transporter GLUT4 to the cell ing the insulin receptor substrate (IRS) proteins that surface membrane by a process called translocation. provide docking sites for p85, the regulatory subunit These plasma membrane-localized transporters sub- of type I phosphatidylinositol 3-kinase (PI3K). This sequently facilitate the influx of plasma glucose into results in the activation of the catalytic p110 subunit the cell. Recent insights into this regulated process of PI3K. Multiple studies using various pharmaco- show that, in addition

Journal

The Journal of Membrane BiologySpringer Journals

Published: Dec 1, 2002

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